1CC8

CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN

1CC8 の概要

• エントリーDOI: 10.2210/pdb1cc8/pdb
• 分子名称: PROTEIN (METALLOCHAPERONE ATX1), MERCURY (II) ION, BENZAMIDINE, ... (4 entities in total)
• 機能のキーワード: copper transport, mercury coordination, metal transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P38636
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8673.54

構造登録者

Rosenzweig, A.C.,Huffman, D.L.,Pufahl, M.Y.R.A.,Hou, T.V.O.,Wernimont, A.K. (登録日: 1999-03-04, 公開日: 1999-12-12, 最終更新日: 2023-12-27)

主引用文献

Rosenzweig, A.C.,Huffman, D.L.,Hou, M.Y.,Wernimont, A.K.,Pufahl, R.A.,O'Halloran, T.V.
Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution.
Structure Fold.Des., 7:605-617, 1999

PubMed Abstract: Metallochaperone proteins function in the trafficking and delivery of essential, yet potentially toxic, metal ions to distinct locations and particular proteins in eukaryotic cells. The Atx1 protein shuttles copper to the transport ATPase Ccc2 in yeast cells. Molecular mechanisms for copper delivery by Atx1 and similar human chaperones have been proposed, but detailed structural characterization is necessary to elucidate how Atx1 binds metal ions and how it might interact with Ccc2 to facilitate metal ion transfer.

PubMed: 10404590
DOI: 10.1016/S0969-2126(99)80082-3

実験手法

X-RAY DIFFRACTION (1.02 Å)